Histone H2B Antibody - #AF0880
Product Info
*The optimal dilutions should be determined by the end user.
*Tips:
WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.
Cite Format: Affinity Biosciences Cat# AF0880, RRID:AB_2834407.
Fold/Unfold
dJ221C16.8; H2B histone family, member A; H2B/a; H2B/g; H2B/h; H2B/k; H2B/l; H2B1C_HUMAN; H2BFA; HIST1H2BI; Histone 1, H2bg; Histone cluster 1 H2B family member g; Histone cluster 1, H2bg; Histone H2B type 1-C/E/F/G/I; Histone H2B.1 A; Histone H2B.a; Histone H2B.g; Histone H2B.h; Histone H2B.k; Histone H2B.l; H2B histone family member R; H2B/r; H2B1J_HUMAN; H2BFR; HIST1H2BJ; Histone 1 H2bj; Histone cluster 1 H2bj; Histone H2B type 1-J; Histone H2B.1; Histone H2B.r; GL105; H2B; H2B histone family member Q; H2B-GL105; H2B.1; H2B/q; H2B2E_HUMAN; H2BFQ; H2BGL105; H2BQ; HIST2H2BE; Histone 2 H2be; histone cluster 2, H2be; histone H2B GL105; histone H2B type 2 E; Histone H2B type 2-E; histone H2B type 2E; Histone H2B-GL105; Histone H2B.q; histone H2BGL105; H2B K; H2B type 12; H2B/b; H2B/c; H2B/d; H2B/e; H2B/f; H2B/j; H2B/n; H2B/q; H2B/r; H2B/s; HIRA-interacting protein 1; HIRA-interacting protein 2; Histone H2B type 1-B; Histone H2B type 1-C/E/F/G/I; Histone H2B type 1-D; Histone H2B type 1-H; Histone H2B type 1-J; Histone H2B type 1-K; Histone H2B type 1-L; Histone H2B type 1-M; Histone H2B type 1-N; Histone H2B type 1-O; Histone H2B type 2-E; Histone H2B type 2-F; Histone H2B type 3-B; Histone H2B type F-S; Histone H2B-GL105; Histone H2B.1 A; Histone H2B.1; Histone H2B.1 B; Histone H2B.2; Histone H2B.a; Histone H2B.b; Histone H2B.c; Histone H2B.d; Histone H2B.e; Histone H2B.f; Histone H2B.g; Histone H2B.h; Histone H2B.j; Histone H2B.k; Histone H2B.l; Histone H2B.n; Histone H2B.r; Histone H2B.s;
Immunogens
A synthesized peptide derived from human Histone H2B, corresponding to a region within C-terminal amino acids.
P62807(H2B1C_HUMAN) >>Visit HPA database.
P06899(H2B1J_HUMAN) >>Visit HPA database.
- P62807 H2B1C_HUMAN:
- Protein BLAST With
- NCBI/
- ExPASy/
- Uniprot
MPEPAKSAPAPKKGSKKAVTKAQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK
- P06899 H2B1J_HUMAN:
- Protein BLAST With
- NCBI/
- ExPASy/
- Uniprot
MPEPAKSAPAPKKGSKKAVTKAQKKDGKKRKRSRKESYSIYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSAK
- Q16778 H2B2E_HUMAN:
- Protein BLAST With
- NCBI/
- ExPASy/
- Uniprot
MPEPAKSAPAPKKGSKKAVTKAQKKDGKKRKRSRKESYSIYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK
- P57053 H2BFS_HUMAN:
- Protein BLAST With
- NCBI/
- ExPASy/
- Uniprot
MPEPAKSAPAPKKGSKKAVTKAQKKDGRKRKRSRKESYSVYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIAGEASRLPHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSAK
PTMs - P62807/P06899/Q16778/P57053 As Substrate
Site | PTM Type | Enzyme | Source |
---|---|---|---|
K6 | Acetylation | Uniprot | |
K6 | Methylation | Uniprot | |
K6 | Sumoylation | Uniprot | |
K6 | Ubiquitination | Uniprot | |
S7 | Phosphorylation | Uniprot | |
K12 | Acetylation | Uniprot | |
K13 | Acetylation | Uniprot | |
S15 | Phosphorylation | Uniprot | |
K16 | Acetylation | Uniprot | |
K17 | Acetylation | Uniprot | |
K21 | Acetylation | Uniprot | |
K21 | Sumoylation | Uniprot | |
K21 | Ubiquitination | Uniprot | |
K24 | Acetylation | Uniprot | |
K25 | Acetylation | Uniprot | |
S33 | Phosphorylation | Uniprot | |
K35 | Acetylation | Uniprot | |
K35 | Ubiquitination | Uniprot | |
S37 | Phosphorylation | Uniprot | |
Y38 | Phosphorylation | Uniprot | |
S39 | Phosphorylation | Uniprot | |
Y41 | Phosphorylation | Uniprot | |
Y43 | Phosphorylation | Uniprot | |
K44 | Acetylation | Uniprot | |
K44 | Methylation | Uniprot | |
K44 | Ubiquitination | Uniprot | |
K47 | Acetylation | Uniprot | |
K47 | Methylation | Uniprot | |
K47 | Sumoylation | Uniprot | |
K47 | Ubiquitination | Uniprot | |
T53 | Phosphorylation | Uniprot | |
S56 | Phosphorylation | Uniprot | |
S57 | Phosphorylation | Uniprot | |
K58 | Acetylation | Uniprot | |
K58 | Methylation | Uniprot | |
K58 | Ubiquitination | Uniprot | |
S65 | Phosphorylation | Uniprot | |
R73 | Methylation | Uniprot | |
R87 | Methylation | Uniprot | |
S88 | Phosphorylation | Uniprot | |
T89 | Phosphorylation | Uniprot | |
S92 | Phosphorylation | Uniprot | |
R93 | Methylation | Uniprot | |
T97 | Phosphorylation | Uniprot | |
R100 | Methylation | Uniprot | |
K109 | Acetylation | Uniprot | |
K109 | Methylation | Uniprot | |
K109 | Sumoylation | Uniprot | |
K109 | Ubiquitination | Uniprot | |
S113 | Phosphorylation | Uniprot | |
T116 | Phosphorylation | Uniprot | |
K117 | Acetylation | Uniprot | |
K117 | Sumoylation | Uniprot | |
K117 | Ubiquitination | Uniprot | |
T120 | Phosphorylation | Uniprot | |
K121 | Acetylation | Uniprot | |
K121 | Sumoylation | Uniprot | |
K121 | Ubiquitination | Uniprot | |
T123 | Phosphorylation | Uniprot | |
S124 | Phosphorylation | Uniprot | |
K126 | Acetylation | Uniprot | |
K126 | Ubiquitination | Uniprot |
Site | PTM Type | Enzyme | Source |
---|---|---|---|
M1 | Acetylation | Uniprot | |
K6 | Acetylation | Uniprot | |
K6 | Methylation | Uniprot | |
K6 | Sumoylation | Uniprot | |
K6 | Ubiquitination | Uniprot | |
S7 | Phosphorylation | Uniprot | |
K12 | Acetylation | Uniprot | |
K13 | Acetylation | Uniprot | |
S15 | Phosphorylation | Uniprot | |
K16 | Acetylation | Uniprot | |
K17 | Acetylation | Uniprot | |
K21 | Acetylation | Uniprot | |
K21 | Sumoylation | Uniprot | |
K21 | Ubiquitination | Uniprot | |
K24 | Acetylation | Uniprot | |
K25 | Acetylation | Uniprot | |
S33 | Phosphorylation | Uniprot | |
K35 | Acetylation | Uniprot | |
K35 | Ubiquitination | Uniprot | |
S37 | Phosphorylation | Uniprot | |
Y38 | Phosphorylation | Uniprot | |
S39 | Phosphorylation | Uniprot | |
Y41 | Phosphorylation | Uniprot | |
Y43 | Phosphorylation | Uniprot | |
K44 | Acetylation | Uniprot | |
K44 | Methylation | Uniprot | |
K44 | Ubiquitination | Uniprot | |
K47 | Acetylation | Uniprot | |
K47 | Methylation | Uniprot | |
K47 | Sumoylation | Uniprot | |
K47 | Ubiquitination | Uniprot | |
T53 | Phosphorylation | Uniprot | |
S56 | Phosphorylation | Uniprot | |
S57 | Phosphorylation | Uniprot | |
K58 | Acetylation | Uniprot | |
K58 | Methylation | Uniprot | |
K58 | Ubiquitination | Uniprot | |
S65 | Phosphorylation | Uniprot | |
R73 | Methylation | Uniprot | |
S79 | Phosphorylation | Uniprot | |
R80 | Methylation | Uniprot | |
Y84 | Phosphorylation | Uniprot | |
K86 | Acetylation | Uniprot | |
K86 | Ubiquitination | Uniprot | |
R87 | Methylation | Uniprot | |
S88 | Phosphorylation | Uniprot | |
T89 | Phosphorylation | Uniprot | |
T91 | Phosphorylation | Uniprot | |
S92 | Phosphorylation | Uniprot | |
R93 | Methylation | Uniprot | |
T97 | Phosphorylation | Uniprot | |
R100 | Methylation | Uniprot | |
K109 | Acetylation | Uniprot | |
K109 | Methylation | Uniprot | |
K109 | Sumoylation | Uniprot | |
K109 | Ubiquitination | Uniprot | |
S113 | O-Glycosylation | Uniprot | |
S113 | Phosphorylation | Uniprot | |
T116 | Phosphorylation | Uniprot | |
K117 | Acetylation | Uniprot | |
K117 | Sumoylation | Uniprot | |
K117 | Ubiquitination | Uniprot | |
T120 | Phosphorylation | Uniprot | |
K121 | Acetylation | Uniprot | |
K121 | Sumoylation | Uniprot | |
K121 | Ubiquitination | Uniprot | |
T123 | Phosphorylation | Uniprot | |
S124 | Phosphorylation | Uniprot | |
K126 | Ubiquitination | Uniprot |
Site | PTM Type | Enzyme | Source |
---|---|---|---|
Acetylation | Uniprot | ||
K6 | Acetylation | Uniprot | |
K6 | Methylation | Uniprot | |
K6 | Sumoylation | Uniprot | |
K6 | Ubiquitination | Uniprot | |
S7 | Phosphorylation | Uniprot | |
K12 | Acetylation | Uniprot | |
K13 | Acetylation | Uniprot | |
S15 | Phosphorylation | Uniprot | |
K16 | Acetylation | Uniprot | |
K17 | Acetylation | Uniprot | |
K21 | Acetylation | Uniprot | |
K21 | Sumoylation | Uniprot | |
K21 | Ubiquitination | Uniprot | |
K24 | Acetylation | Uniprot | |
K35 | Ubiquitination | Uniprot | |
S37 | Phosphorylation | Uniprot | |
Y38 | Phosphorylation | Uniprot | |
S39 | Phosphorylation | Uniprot | |
Y41 | Phosphorylation | Uniprot | |
Y43 | Phosphorylation | Uniprot | |
K44 | Acetylation | Uniprot | |
K44 | Ubiquitination | Uniprot | |
K47 | Acetylation | Uniprot | |
K47 | Methylation | Uniprot | |
K47 | Sumoylation | Uniprot | |
K47 | Ubiquitination | Uniprot | |
T53 | Phosphorylation | Uniprot | |
S56 | Phosphorylation | Uniprot | |
S57 | Phosphorylation | Uniprot | |
K58 | Methylation | Uniprot | |
K58 | Ubiquitination | Uniprot | |
S65 | Phosphorylation | Uniprot | |
R73 | Methylation | Uniprot | |
S79 | Phosphorylation | Uniprot | |
R80 | Methylation | Uniprot | |
Y84 | Phosphorylation | Uniprot | |
K86 | Ubiquitination | Uniprot | |
R87 | Methylation | Uniprot | |
S88 | Phosphorylation | Uniprot | |
T89 | Phosphorylation | Uniprot | |
S92 | Phosphorylation | Uniprot | |
R93 | Methylation | Uniprot | |
T97 | Phosphorylation | Uniprot | |
R100 | Methylation | Uniprot | |
K109 | Acetylation | Uniprot | |
K109 | Methylation | Uniprot | |
K109 | Sumoylation | Uniprot | |
K109 | Ubiquitination | Uniprot | |
S113 | Phosphorylation | Uniprot | |
T116 | Phosphorylation | Uniprot | |
K117 | Acetylation | Uniprot | |
K117 | Sumoylation | Uniprot | |
K117 | Ubiquitination | Uniprot | |
T120 | Phosphorylation | Uniprot | |
K121 | Acetylation | Uniprot | |
K121 | Sumoylation | Uniprot | |
K121 | Ubiquitination | Uniprot | |
T123 | Phosphorylation | Uniprot | |
S124 | Phosphorylation | Uniprot | |
K126 | Ubiquitination | Uniprot |
Site | PTM Type | Enzyme | Source |
---|---|---|---|
Acetylation | Uniprot | ||
M1 | Acetylation | Uniprot | |
K6 | Acetylation | Uniprot | |
K6 | Methylation | Uniprot | |
K6 | Sumoylation | Uniprot | |
K6 | Ubiquitination | Uniprot | |
S7 | Phosphorylation | Uniprot | |
K12 | Acetylation | Uniprot | |
K13 | Acetylation | Uniprot | |
S15 | Phosphorylation | Uniprot | |
K16 | Acetylation | Uniprot | |
K17 | Acetylation | Uniprot | |
K21 | Acetylation | Uniprot | |
K21 | Sumoylation | Uniprot | |
K21 | Ubiquitination | Uniprot | |
K24 | Acetylation | Uniprot | |
K25 | Acetylation | Uniprot | |
K35 | Ubiquitination | Uniprot | |
S37 | Phosphorylation | Uniprot | |
Y38 | Phosphorylation | Uniprot | |
S39 | Phosphorylation | Uniprot | |
Y41 | Phosphorylation | Uniprot | |
Y43 | Phosphorylation | Uniprot | |
K44 | Acetylation | Uniprot | |
K44 | Ubiquitination | Uniprot | |
K47 | Acetylation | Uniprot | |
K47 | Methylation | Uniprot | |
K47 | Sumoylation | Uniprot | |
K47 | Ubiquitination | Uniprot | |
T53 | Phosphorylation | Uniprot | |
S56 | Phosphorylation | Uniprot | |
S57 | Phosphorylation | Uniprot | |
K58 | Acetylation | Uniprot | |
K58 | Methylation | Uniprot | |
K58 | Ubiquitination | Uniprot | |
S65 | Phosphorylation | Uniprot | |
R73 | Methylation | Uniprot | |
S79 | Phosphorylation | Uniprot | |
R80 | Methylation | Uniprot | |
Y84 | Phosphorylation | Uniprot | |
K86 | Acetylation | Uniprot | |
K86 | Ubiquitination | Uniprot | |
R87 | Methylation | Uniprot | |
S88 | Phosphorylation | Uniprot | |
T89 | Phosphorylation | Uniprot | |
T91 | Phosphorylation | Uniprot | |
S92 | Phosphorylation | Uniprot | |
R93 | Methylation | Uniprot | |
T97 | Phosphorylation | Uniprot | |
R100 | Methylation | Uniprot | |
K109 | Acetylation | Uniprot | |
K109 | Methylation | Uniprot | |
K109 | Sumoylation | Uniprot | |
K109 | Ubiquitination | Uniprot | |
S113 | Phosphorylation | Uniprot | |
T116 | Phosphorylation | Uniprot | |
K117 | Acetylation | Uniprot | |
K117 | Sumoylation | Uniprot | |
K117 | Ubiquitination | Uniprot | |
T120 | Phosphorylation | Uniprot | |
K121 | Acetylation | Uniprot | |
K121 | Sumoylation | Uniprot | |
K121 | Ubiquitination | Uniprot | |
Y122 | Phosphorylation | Uniprot | |
T123 | Phosphorylation | Uniprot | |
S124 | Phosphorylation | Uniprot | |
K126 | Acetylation | Uniprot | |
K126 | Ubiquitination | Uniprot |
Research Backgrounds
Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
Has broad antibacterial activity. May contribute to the formation of the functional antimicrobial barrier of the colonic epithelium, and to the bactericidal activity of amniotic fluid.
Monoubiquitination at Lys-35 (H2BK34Ub) by the MSL1/MSL2 dimer is required for histone H3 'Lys-4' (H3K4me) and 'Lys-79' (H3K79me) methylation and transcription activation at specific gene loci, such as HOXA9 and MEIS1 loci. Similarly, monoubiquitination at Lys-121 (H2BK120Ub) by the RNF20/40 complex gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation. It also functions cooperatively with the FACT dimer to stimulate elongation by RNA polymerase II. H2BK120Ub also acts as a regulator of mRNA splicing: deubiquitination by USP49 is required for efficient cotranscriptional splicing of a large set of exons.
Phosphorylation at Ser-37 (H2BS36ph) by AMPK in response to stress promotes transcription (By similarity). Phosphorylated on Ser-15 (H2BS14ph) by STK4/MST1 during apoptosis; which facilitates apoptotic chromatin condensation. Also phosphorylated on Ser-15 in response to DNA double strand breaks (DSBs), and in correlation with somatic hypermutation and immunoglobulin class-switch recombination.
GlcNAcylation at Ser-113 promotes monoubiquitination of Lys-121. It fluctuates in response to extracellular glucose, and associates with transcribed genes.
Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes.
Nucleus. Chromosome.
The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA.
Belongs to the histone H2B family.
Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
Has broad antibacterial activity. May contribute to the formation of the functional antimicrobial barrier of the colonic epithelium, and to the bactericidal activity of amniotic fluid.
Monoubiquitination at Lys-35 (H2BK34Ub) by the MSL1/MSL2 dimer is required for histone H3 'Lys-4' (H3K4me) and 'Lys-79' (H3K79me) methylation and transcription activation at specific gene loci, such as HOXA9 and MEIS1 loci. Similarly, monoubiquitination at Lys-121 (H2BK120Ub) by the RNF20/40 complex gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation. It also functions cooperatively with the FACT dimer to stimulate elongation by RNA polymerase II. H2BK120Ub also acts as a regulator of mRNA splicing: deubiquitination by USP49 is required for efficient cotranscriptional splicing of a large set of exons.
Phosphorylation at Ser-37 (H2BS36ph) by AMPK in response to stress promotes transcription (By similarity). Phosphorylated on Ser-15 (H2BS14ph) by STK4/MST1 during apoptosis; which facilitates apoptotic chromatin condensation. Also phosphorylated on Ser-15 in response to DNA double strand breaks (DSBs), and in correlation with somatic hypermutation and immunoglobulin class-switch recombination.
GlcNAcylation at Ser-113 promotes monoubiquitination of Lys-121. It fluctuates in response to extracellular glucose, and associates with transcribed genes (By similarity).
Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes.
Nucleus. Chromosome.
The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA. Heterodimer H2BC11 and H2AZ1 interacts with VPS72 (via N-terminal domain).
Belongs to the histone H2B family.
Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
Has broad antibacterial activity. May contribute to the formation of the functional antimicrobial barrier of the colonic epithelium, and to the bactericidal activity of amniotic fluid.
Monoubiquitination at Lys-35 (H2BK34Ub) by the MSL1/MSL2 dimer is required for histone H3 'Lys-4' (H3K4me) and 'Lys-79' (H3K79me) methylation and transcription activation at specific gene loci, such as HOXA9 and MEIS1 loci. Similarly, monoubiquitination at Lys-121 (H2BK120Ub) by the RNF20/40 complex gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation. It also functions cooperatively with the FACT dimer to stimulate elongation by RNA polymerase II. H2BK120Ub also acts as a regulator of mRNA splicing: deubiquitination by USP49 is required for efficient cotranscriptional splicing of a large set of exons.
Phosphorylation at Ser-37 (H2BS36ph) by AMPK in response to stress promotes transcription (By similarity). Phosphorylated on Ser-15 (H2BS14ph) by STK4/MST1 during apoptosis; which facilitates apoptotic chromatin condensation. Also phosphorylated on Ser-15 in response to DNA double strand breaks (DSBs), and in correlation with somatic hypermutation and immunoglobulin class-switch recombination.
GlcNAcylation at Ser-113 promotes monoubiquitination of Lys-121. It fluctuates in response to extracellular glucose, and associates with transcribed genes (By similarity).
Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes.
Nucleus. Chromosome.
The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA.
Belongs to the histone H2B family.
Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
Has broad antibacterial activity. May contribute to the formation of the functional antimicrobial barrier of the colonic epithelium, and to the bactericidal activity of amniotic fluid.
Monoubiquitination at Lys-35 (H2BK34Ub) by the MSL1/MSL2 dimer is required for histone H3 'Lys-4' (H3K4me) and 'Lys-79' (H3K79me) methylation and transcription activation at specific gene loci, such as HOXA9 and MEIS1 loci. Similarly, monoubiquitination at Lys-121 (H2BK120Ub) by the RNF20/40 complex gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation. It also functions cooperatively with the FACT dimer to stimulate elongation by RNA polymerase II. H2BK120Ub also acts as a regulator of mRNA splicing: deubiquitination by USP49 is required for efficient cotranscriptional splicing of a large set of exons.
Phosphorylation at Ser-37 (H2BS36ph) by AMPK in response to stress promotes transcription (By similarity). Phosphorylated on Ser-15 (H2BS14ph) by STK4/MST1 during apoptosis; which facilitates apoptotic chromatin condensation. Also phosphorylated on Ser-15 in response to DNA double strand breaks (DSBs), and in correlation with somatic hypermutation and immunoglobulin class-switch recombination.
GlcNAcylation at Ser-113 promotes monoubiquitination of Lys-121. It fluctuates in response to extracellular glucose, and associates with transcribed genes (By similarity).
Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes.
Nucleus. Chromosome.
The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA.
Belongs to the histone H2B family.
Research Fields
· Human Diseases > Substance dependence > Alcoholism.
· Human Diseases > Cancers: Overview > Viral carcinogenesis.
· Human Diseases > Immune diseases > Systemic lupus erythematosus.
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